RNAS1_PONPY
ID RNAS1_PONPY Reviewed; 156 AA.
AC Q8SQ12; Q1KHR1; Q5R5A9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Ribonuclease pancreatic;
DE EC=4.6.1.18;
DE AltName: Full=RNase 1;
DE AltName: Full=RNase A;
DE Flags: Precursor;
GN Name=RNASE1; Synonyms=RNS1;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11925567; DOI=10.1038/ng852;
RA Zhang J., Zhang Y.-P., Rosenberg H.F.;
RT "Adaptive evolution of a duplicated pancreatic ribonuclease gene in a leaf-
RT eating monkey.";
RL Nat. Genet. 30:411-415(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16751256; DOI=10.1093/molbev/msl025;
RA Schienman J.E., Holt R.A., Auerbach M.R., Stewart C.B.;
RT "Duplication and divergence of two distinct pancreatic ribonuclease genes
RT in leaf-eating African and Asian colobine monkeys.";
RL Mol. Biol. Evol. 23:1465-1479(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3'
CC side of pyrimidine nucleotides. Acts on single-stranded and double-
CC stranded RNA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC -!- SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes with
CC RNH1. Dimerization of two such complexes may occur. Interaction with
CC RNH1 inhibits this protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Pancreas and other tissues and body fluids
CC (indicating it may have other physiological functions besides its role
CC in digestion).
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AF449630; AAL87051.1; -; Genomic_DNA.
DR EMBL; DQ494868; ABF00145.1; -; Genomic_DNA.
DR EMBL; CR860954; CAH93057.1; -; mRNA.
DR AlphaFoldDB; Q8SQ12; -.
DR SMR; Q8SQ12; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..156
FT /note="Ribonuclease pancreatic"
FT /id="PRO_0000030937"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..112
FT /evidence="ECO:0000250"
FT DISULFID 68..123
FT /evidence="ECO:0000250"
FT DISULFID 86..138
FT /evidence="ECO:0000250"
FT DISULFID 93..100
FT /evidence="ECO:0000250"
FT CONFLICT 129
FT /note="T -> P (in Ref. 3; CAH93057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17608 MW; C87B07BF46B1F141 CRC64;
MALEKSLVLL PLLVLILLVL GWVQPSLGKE SRAKKFQRQH MDSGSSPNSN STYCNQMMRR
RNMTQGRCKP VNTFVHEPLV DVQNVCFQEK VTCKNGQGNC YKSNSSMHIT DCRLTHGSRY
PNCAYRTSTK ERHIIVACEG SPYVPVHFDA SVEDST